Involvement of the Saccharomyces cerevisiae hydrolase Ldh1p in lipid homeostasis

Eukaryot Cell. 2011 Jun;10(6):776-81. doi: 10.1128/EC.05040-11. Epub 2011 Apr 8.

Abstract

Here, we report the functional characterization of the newly identified lipid droplet hydrolase Ldh1p. Recombinant Ldh1p exhibits esterase and triacylglycerol lipase activities. Mutation of the serine in the hydrolase/lipase motif GXSXG completely abolished esterase activity. Ldh1p is required for the maintenance of a steady-state level of the nonpolar and polar lipids of lipid droplets. A characteristic feature of the Saccharomyces cerevisiae Δldh1 strain is the appearance of giant lipid droplets and an excessive accumulation of nonpolar lipids and phospholipids upon growth on medium containing oleic acid as a sole carbon source. Ldh1p is thought to play a role in maintaining the lipid homeostasis in yeast by regulating both phospholipid and nonpolar lipid levels.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs / genetics
  • Amino Acid Sequence
  • Enzyme Assays
  • Esterases / metabolism
  • Gene Knockout Techniques
  • Lipid Metabolism*
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Organelle Size / genetics
  • Organelles / metabolism
  • Organelles / ultrastructure
  • Phospholipases A / genetics
  • Phospholipases A / isolation & purification
  • Phospholipases A / metabolism*
  • Protein Transport / genetics
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / isolation & purification
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Alignment

Substances

  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Esterases
  • Ldh1 protein, S cerevisiae
  • Phospholipases A